Abstract
The beauty, symmetry, and functionality of icosahedral virus capsids has attracted the attention of biologists, physicists, and mathematicians ever since they were first observed. Viruses and protein cages assemble into functional architectures in a range of sizes, shapes, and symmetries. To fulfill their biological roles, these structures must self-assemble, resist stress, and are often dynamic. The increasing use of icosahedral capsids and cages in materials science has driven the need to quantify them in terms of structural properties such as rigidity, stiffness, and viscoelasticity. In this study, we employed Quartz Crystal Microbalance with Dissipation technology (QCM-D) to characterize and compare the mechanical rigidity of different protein cages and viruses. We attempted to unveil the relationships between rigidity, radius, shell thickness, and triangulation number. We show that the rigidity and triangulation numbers are inversely related to each other and the comparison of rigidity and radius also follows the same trend. Our results suggest that subunit orientation, protein–protein interactions, and protein–nucleic acid interactions are important for the resistance to deformation of these complexes, however, the relationships are complex and need to be explored further. The QCM-D based viscoelastic measurements presented here help us elucidate these relationships and show the future prospect of this technique in the field of physical virology and nano-biotechnology.
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Acknowledgements
We thank Dr. Matthew Dixon from Biolin Scientific for technical assistance. We also thank Ms. Neerja Zambare for insightful discussions. We thank Drs. David D Dunnigan, James L. Van Etten, Trevor Douglas, John E. Johnson, Adam Zlotnick, and Mavis McKenna for providing the samples for this analysis. This project was funded in part by NIH AAV grant R01 AI081961-01A1 to BB.
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Kant, R., Rayaprolu, V., McDonald, K. et al. Curating viscoelastic properties of icosahedral viruses, virus-based nanomaterials, and protein cages. J Biol Phys 44, 211–224 (2018). https://doi.org/10.1007/s10867-018-9491-x
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DOI: https://doi.org/10.1007/s10867-018-9491-x